The interwinding nature of protein-protein interfaces and its implication for protein complex formation

Yura, Kei and Hayward, Steven ORCID: https://orcid.org/0000-0001-6959-2604 (2009) The interwinding nature of protein-protein interfaces and its implication for protein complex formation. Bioinformatics, 25 (23). pp. 3108-3113. ISSN 1367-4803

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Abstract

Motivation: Structural features at protein–protein interfaces can be studied to understand protein–protein interactions. It was noticed that in a dataset of 45 multimeric proteins the interface could either be described as flat against flat or protruding/interwound. In the latter, residues within one chain were surrounded by those in other chains, whereas in the former they were not. Results: A simple method was developed that could distinguish between these two types with results that matched those made by a human annotator. Applying this automatic method to a large dataset of 888 structures, chains at interfaces were categorized as non-surrounded or surrounded. It was found that the surrounded set had a significantly lower folding tendency using a sequence based measure, than the non-surrounded set. This suggests that before complexation, surrounded chains are relatively unstable and may be involved in ‘fly-casting’. This is supported by the finding that terminal regions are overrepresented in the surrounded set. Availability:http://cib.cf.ocha.ac.jp/DACSIS/

Item Type: Article
Faculty \ School: Faculty of Science > School of Computing Sciences
Faculty of Science > School of Biological Sciences
Depositing User: Vishal Gautam
Date Deposited: 10 Mar 2011 10:44
Last Modified: 03 Oct 2022 00:41
URI: https://ueaeprints.uea.ac.uk/id/eprint/22561
DOI: 10.1093/bioinformatics/btp563

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